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J. Biol. Chem., Vol. 276, Issue 10, 7661-7671, March 9, 2001
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From the Physiological Laboratory, University of Liverpool,
Liverpool L69 3BX, United Kingdom
Vesicular monoamine transporter 2 is important
for the accumulation of monoamine neurotransmitters into synaptic
vesicles and histamine transport into secretory vesicles of the
enterochromaffin-like cell of the gastric corpus. In this study we have
investigated the mechanisms regulating the transcriptional activation
of the rat vesicular monoamine transporter 2 (VMAT2) promoter in
gastric epithelial cells. Maintenance of basal levels of transcription was dependent on the presence of SP1, cAMP-response element (CRE), and
overlapping AP2/SP1 consensus sequences within the region of promoter
from
Transcriptional Activation of the Rat Vesicular
Monoamine Transporter 2 Promoter in Gastric Epithelial Cells
REGULATION BY GASTRIN*
,
86 to +1 base pairs (bp). Gastrin stimulation increased
transcriptional activity, and responsiveness was shown to be dependent
on the CRE (33 to 26 bp) and AP2/SP1 (61 to 48 bp) consensus
sites but independent of the SP1 site at 86 to 81 bp.
Gastrin-induced transcription was dependent on the cooperative
interaction of an uncharacterized nuclear factor of ~23.3 kDa that
bound to the putative AP2/SP1 site, CRE-binding protein (CREB), and
CREB-binding protein/p300. Gastrin stimulation resulted in the
increased binding of phosphorylated CREB to the promoter, but it did
not result in the increased binding of the AP2/SP1-binding protein. The
gastrin responsiveness of the promoter was shown to be dependent on
both the protein kinase C and mitogen-activated protein
kinase/extracellular signal-regulated kinase kinase-signaling pathways,
which may converge on the AP2/SP1-binding protein.
*
This work was supported by Wellcome Trust Grant 050830.The costs of publication of this
article were defrayed in part by the payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: The Physiological
Laboratory, University of Liverpool, Crown St., Liverpool L69 3BX, UK.
E-mail: watso@liv.ac.uk.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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